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Protein Sci. 2007 Nov;16(11):2317-33.

Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.

Author information

1
Chemistry Department, Princeton University, NJ 08544-1009, USA. jcarey@princeton.edu

Abstract

The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.

PMID:
17962398
PMCID:
PMC2211703
DOI:
10.1110/ps.072985007
[Indexed for MEDLINE]
Free PMC Article

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